title: Structure of a dimeric fungal α-type carbonic anhydrase.
abstract: The crystal structure of Aspergillus oryzae carbonic anhydrase (AoCA) was determined at 2.7Å resolution and it revealed a dimer, which only has precedents in the α class in two membrane and cancer-associated enzymes. α carbonic anhydrases are underrepresented in fungi compared to the β class, this being the first structural representative. The overall fold and zinc binding site resemble other well studied carbonic anhydrases. A major difference is that the histidine, thought to be the major proton shuttle residue in most mammalian enzymes, is replaced by a phenylalanine in AoCA. This finding poses intriguing questions as to the biological functions of fungal α carbonic anhydrases, which are promising candidates for biotechnological applications.
authors.affiliation: Department of Chemistry, University of Copenhagen, Copenhagen, Denmark.
authors.forename: Jose Antonio
authors.initials: JA
authors.lastname: Cuesta-Seijo
authors.forename: Martin Simon
authors.initials: MS
authors.lastname: Borchert
authors.forename: Jens-Christian
authors.initials: JC
authors.lastname: Navarro-Poulsen
authors.forename: Kirk Matthew
authors.initials: KM
authors.lastname: Schnorr
authors.forename: Steen Bennike
authors.initials: SB
authors.lastname: Mortensen
authors.forename: Leila
authors.initials: L
authors.lastname: Lo Leggio
mesh_terms: D000595:Amino Acid Sequence; D001236:Aspergillus oryzae / Q000201:enzymology*; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary
chemical_list: D002256:Carbonic Anhydrases